ID W4UZC3_9BACE Unreviewed; 436 AA.
AC W4UZC3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Phenylacetate-coenzyme A ligase {ECO:0000256|PIRNR:PIRNR006444};
DE EC=6.2.1.30 {ECO:0000256|PIRNR:PIRNR006444};
DE AltName: Full=Phenylacetyl-CoA ligase {ECO:0000256|PIRNR:PIRNR006444};
GN ORFNames=JCM10512_5136 {ECO:0000313|EMBL:GAE86610.1};
OS Bacteroides reticulotermitis JCM 10512.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE86610.1, ECO:0000313|Proteomes:UP000019131};
RN [1] {ECO:0000313|EMBL:GAE86610.1, ECO:0000313|Proteomes:UP000019131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE86610.1,
RC ECO:0000313|Proteomes:UP000019131};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT Isolated from the Gut of a Termite.";
RL Genome Announc. 2:e00072-14(2014).
CC -!- FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to
CC phenylacetyl-CoA (PA-CoA). {ECO:0000256|PIRNR:PIRNR006444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylacetate + ATP + CoA = AMP + diphosphate +
CC phenylacetyl-CoA; Xref=Rhea:RHEA:20956, ChEBI:CHEBI:18401,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57390, ChEBI:CHEBI:456215; EC=6.2.1.30;
CC Evidence={ECO:0000256|PIRNR:PIRNR006444};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC {ECO:0000256|PIRNR:PIRNR006444}.
CC -!- SIMILARITY: Belongs to the phenylacetyl-CoA ligase family.
CC {ECO:0000256|PIRNR:PIRNR006444}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAE86610.1}.
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DR EMBL; BAIV01000059; GAE86610.1; -; Genomic_DNA.
DR RefSeq; WP_044165786.1; NZ_BAIV01000059.1.
DR AlphaFoldDB; W4UZC3; -.
DR STRING; 1445607.JCM10512_5136; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000019131; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0047475; F:phenylacetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0010124; P:phenylacetate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05913; PaaK; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR028154; AMP-dep_Lig_C.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011880; PA_CoA_ligase.
DR PANTHER; PTHR43845; BLR5969 PROTEIN; 1.
DR PANTHER; PTHR43845:SF1; BLR5969 PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF14535; AMP-binding_C_2; 1.
DR PIRSF; PIRSF006444; PaaK; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|PIRNR:PIRNR006444, ECO:0000313|EMBL:GAE86610.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000019131}.
FT DOMAIN 90..287
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 337..432
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 436 AA; 49390 MW; 58DE6C83063F602F CRC64;
MSTEYWEEEI ETAPRSKLEE LQLQRLKKTI NLAANSPYYK EVFSQNNITK DSIQTLSDIR
KIPFTTKVDM RAHYPFGLVA GDMRNDGVRI HSSSGTTGNP TVIVHSQHDI DSWANLVARC
LYMVGIRKTD VFQNSSGYGM FTGGLGFQYG AERLGCLTIP AAAGNSKRQI KFINDFKTTA
LHAIPSYAIR LAEILQEEGI DPQSTTLKTL VIGAEPHTDE QRRKIEQLLG VKAYNSFGMT
EMNGPGVAFE CQNQDGMHFW EDCYFVEIID PETGEQLPEG EIGELVLTTL DREMMPLIRY
RTRDLTRIIP GKCSCGRTHL RIDRIQGRSD DMFIIKGVNI FPMQVEKILV QFPQLGSNYL
ITLETVDNQD EMVVEVELSN LSSDNYIDLE RIRKNITRQL KDEILVTPKV KLVKKGSLPE
SEGKAVRVKD RRDNKS
//
